Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Immunological characterization of the purine-cytosine permease of Saccharomyces cerevisiae: evidence of in vivo phosphorylation of the carrier.

Folia microbiologica - 1 Jan 1996

Pinson B, Pillois X, Brèthes D, Chevallier J, Napias C

Abstract excerpt

No abstract is available from the source.

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acids
Share to Antibodies, Fungal
Share to Blotting, Western
Share to Electrophoresis, Polyacrylamide Gel

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Fungal Proteins

Share to Membrane Transport Proteins

Share to Peptides

Share to Precipitin Tests

Source

Identifiers

PMID: 9090850
DOI: 10.1007/BF02816368

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Immunological characterization of the purine-cytosine permease of Saccharomyces cerevisiae: evidence of in vivo phosphorylation of the carrier.PMID 9090850Read ↗

Functional analyses of yeast purine-cytosine permease mutants.Semantic proximity Read ↗

Screening of an intragenic second-site suppressor of purine-cytosine permease from Saccharomyces cerevisiae. Possible role of Ser272 in the base translocation process.Semantic proximity Read ↗

Evidence for a dynamic role for proline376 in the purine-cytosine permease of Saccharomyces cerevisiae.Semantic proximity Read ↗

Functional analysis of mutated purine-cytosine permease from Saccharomyces cerevisiae. A possible role of the hydrophilic segment 371-377 in the active carrier conformation.Semantic proximity Read ↗

Determination of a specific region of the purine-cytosine permease involved in the recognition of its substrates.Semantic proximity Read ↗

In vivo and in vitro studies of the purine-cytosine permease of Saccharomyces cerevisiae. Functional analysis of a mutant with an altered apparent transport constant of uptake.Semantic proximity Read ↗

Phosphorylation of yeast phosphatidylserine synthase by protein kinase A: identification of Ser46 and Ser47 as major sites of phosphorylation.Semantic proximity Read ↗

Replacement of Lys by Glu in a transmembrane segment strongly impairs the function of the uracil permease from Saccharomyces cerevisiae.Semantic proximity Read ↗

The purine-cytosine permease gene of Saccharomyces cerevisiae: primary structure and deduced protein sequence of the FCY2 gene product.Semantic proximity Read ↗

Maturation of the yeast plasma membrane [H+]ATPase involves phosphorylation during intracellular transport.Semantic proximity Read ↗

Phosphoglucomutase in Saccharomyces cerevisiae is a cytoplasmic glycoprotein and the acceptor for a Glc-phosphotransferase.Semantic proximity Read ↗

Identification of catalytic residues in the beta-glucoside permease of Escherichia coli by site-specific mutagenesis and demonstration of interdomain cross-reactivity between the beta-glucoside and glucose systems.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.